Ovomucin is a mucin-type glycoprotein accounting for 3.5% (w/w) of total egg white proteins. The purpose of the study was to explore the potential of ovomucin as a protein-resistant material. Using bovine serum albumin (BSA) as a model protein, ovomucin decreased the fluorescence intensities of the adsorbed BSA from 10.90 ± 2.18 to 0.67 ± 0.75, indicating its protein-resistant property. To understand the underlying mechanism, pure repulsive forces between ovomucin and model proteins (e.g., BSA and ovomucin) at various pHs (2.0, 6.0, and 7.2) and ionic strengths (0.1, 10, and 150 mM NaCl) were measured using a surface forces apparatus. Further studies by using atomic force microscope imaging, zeta potential, and dynamic light scattering suggested that the protein-resistant property of ovomucin was mainly attributed to strong electrostatic and steric repulsions between protein layers. This work has demonstrated that ovomucin has antifouling potential with broad applications in the areas of food processing industry and biomedical implants.
Keywords: electrostatic and steric repulsions; ionic strength; ovomucin; pH; protein-resistant property.